Abstract
Cellulase is an efficient enzymatic catalyst that hydrolyses cellulosic substances. The high costs associated with using enzymes for industrial applications can be reduced by immobilizing the cellulase. In the current study, cellulase produced by Aspergillus fumigatus JCF was immobilized onto MnO2 nanoparticles, which improve the activity of cellulase and offer a superior support. The surface characteristics of synthesized MnO2 nanoparticles and cellulase-bound MnO2 nanoparticles were investigated by scanning electron microscopy, and Fourier transform infrared spectroscopy was used to analyze the functional characteristics of the immobilized cellulase. The maximum cellulase binding efficiency was 75%. The properties of the immobilized cellulase, including activity, operational pH, temperature, thermal stability, and reusability were investigated and were found to be more stable than for the free enzyme. It was found that cellulase immobilized on MnO2 nanoparticles could be used to hydrolyze cellulosic substances over a broad range of temperature and pH. The results confirmed that cellulase immobilized on MnO2 nanoparticles was very efficient in terms of cellulolytic activity.
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